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P14922

- CYC8_YEAST

UniProt

P14922 - CYC8_YEAST

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Protein

General transcriptional corepressor CYC8

Gene

CYC8

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

Acts as component of the CYC8-TUP1 corepressor complex which is involved in the repression of many genes in a wide variety of physiological processes including heme-regulated and catabolite repressed genes. May also be involved in the derepression of at least some target genes. The complex is recruited to target genes by interaction with DNA-bound transcriptional repressors, like MATALPHA2, MIG1, RFX1 and SKO1. The complex recruits histone deacetylases to produce a repressive chromatin structure, interacts with hypoacetylated N-terminal tails of histones H3 and H4 that have been programmed for repression by the action of histone deacetylases and interferes directly with the transcriptional machinery by associating with the RNA polymerase II mediator complex.5 Publications

GO - Molecular functioni

  1. histone deacetylase binding Source: SGD
  2. RNA polymerase II transcription factor binding transcription factor activity involved in negative regulation of transcription Source: SGD
  3. RNA polymerase II transcription factor binding transcription factor activity involved in positive regulation of transcription Source: SGD

GO - Biological processi

  1. chromatin remodeling Source: SGD
  2. negative regulation of dipeptide transport by negative regulation of transcription from RNA polymerase II promoter Source: SGD
  3. negative regulation of transcription from RNA polymerase II promoter Source: SGD
  4. negative regulation of transcription from RNA polymerase II promoter during mitosis Source: SGD
  5. nucleosome positioning Source: SGD
  6. positive regulation of transcription from RNA polymerase II promoter Source: GOC
  7. regulation of fatty acid biosynthetic process by regulation of transcription from RNA polymerase II promoter Source: SGD
  8. regulation of response to DNA damage stimulus Source: SGD
Complete GO annotation...

Keywords - Molecular functioni

Prion, Repressor

Keywords - Biological processi

Transcription, Transcription regulation

Enzyme and pathway databases

BioCyciYEAST:G3O-29073-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
General transcriptional corepressor CYC8
Alternative name(s):
Glucose repression mediator protein CYC8
Gene namesi
Name:CYC8
Synonyms:CRT8, SSN6
Ordered Locus Names:YBR112C
ORF Names:YBR0908
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
ProteomesiUP000002311: Chromosome II

Organism-specific databases

SGDiS000000316. CYC8.

Subcellular locationi

GO - Cellular componenti

  1. nucleus Source: SGD
  2. transcriptional repressor complex Source: SGD
Complete GO annotation...

Keywords - Cellular componenti

Amyloid, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 966966General transcriptional corepressor CYC8PRO_0000106327Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei429 – 4291Phosphoserine2 Publications
Modified residuei475 – 4751Phosphothreonine1 Publication
Modified residuei710 – 7101Phosphoserine1 Publication
Modified residuei741 – 7411Phosphoserine1 Publication
Modified residuei768 – 7681Phosphoserine1 Publication
Modified residuei815 – 8151Phosphoserine2 Publications
Modified residuei817 – 8171Phosphoserine2 Publications
Modified residuei866 – 8661Phosphoserine1 Publication
Modified residuei943 – 9431Phosphoserine3 Publications

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiP14922.
PaxDbiP14922.
PeptideAtlasiP14922.

Expressioni

Gene expression databases

GenevestigatoriP14922.

Interactioni

Subunit structurei

Associates with TUP1 to form the CYC8-TUP1 (or TUP1-SSN6) corepressor complex that is composed of 4 copies of TUP1 and one copy of CYC8. Interacts with MATALPHA2, CTI6, MIG1, TUP1, SUT1, RFX1, PGD1, HOS1, HOS2 AND RPD3.10 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
HOS2P530964EBI-18215,EBI-8475
PGD1P403563EBI-18215,EBI-13268
RFX1P487432EBI-18215,EBI-15036
RPD3P325616EBI-18215,EBI-15864
TUP1P166495EBI-18215,EBI-19654

Protein-protein interaction databases

BioGridi32816. 103 interactions.
DIPiDIP-696N.
IntActiP14922. 10 interactions.
MINTiMINT-579675.
STRINGi4932.YBR112C.

Structurei

3D structure databases

ProteinModelPortaliP14922.
SMRiP14922. Positions 46-395.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati46 – 7934TPR 1Add
BLAST
Repeati80 – 11334TPR 2Add
BLAST
Repeati114 – 14734TPR 3Add
BLAST
Repeati150 – 18334TPR 4Add
BLAST
Repeati187 – 22034TPR 5Add
BLAST
Repeati224 – 25734TPR 6Add
BLAST
Repeati262 – 29534TPR 7Add
BLAST
Repeati296 – 32934TPR 8Add
BLAST
Repeati330 – 36334TPR 9Add
BLAST
Repeati364 – 39835TPR 10Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni467 – 682216Prion domain (PrD)Add
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi15 – 3016Poly-GlnAdd
BLAST

Domaini

The prion domain (PrD) is a Gln/Asn (Q/N)-rich domain, which is unstructured in its native, soluble form, and which forms a parallel in-register beta-sheet in its amyloid form.By similarity

Sequence similaritiesi

Belongs to the CYC8/SSN6 family.Curated
Contains 10 TPR repeats.PROSITE-ProRule annotation

Keywords - Domaini

Repeat, TPR repeat

Phylogenomic databases

eggNOGiCOG0457.
GeneTreeiENSGT00410000025758.
InParanoidiP14922.
KOiK06665.
OrthoDBiEOG7NKKW1.

Family and domain databases

Gene3Di1.25.40.10. 2 hits.
InterProiIPR013026. TPR-contain_dom.
IPR011990. TPR-like_helical_dom.
IPR001440. TPR_1.
IPR019734. TPR_repeat.
[Graphical view]
PfamiPF00515. TPR_1. 6 hits.
[Graphical view]
SMARTiSM00028. TPR. 10 hits.
[Graphical view]
PROSITEiPS50005. TPR. 9 hits.
PS50293. TPR_REGION. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P14922-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MNPGGEQTIM EQPAQQQQQQ QQQQQQQQQQ AAVPQQPLDP LTQSTAETWL
60 70 80 90 100
SIASLAETLG DGDRAAMAYD ATLQFNPSSA KALTSLAHLY RSRDMFQRAA
110 120 130 140 150
ELYERALLVN PELSDVWATL GHCYLMLDDL QRAYNAYQQA LYHLSNPNVP
160 170 180 190 200
KLWHGIGILY DRYGSLDYAE EAFAKVLELD PHFEKANEIY FRLGIIYKHQ
210 220 230 240 250
GKWSQALECF RYILPQPPAP LQEWDIWFQL GSVLESMGEW QGAKEAYEHV
260 270 280 290 300
LAQNQHHAKV LQQLGCLYGM SNVQFYDPQK ALDYLLKSLE ADPSDATTWY
310 320 330 340 350
HLGRVHMIRT DYTAAYDAFQ QAVNRDSRNP IFWCSIGVLY YQISQYRDAL
360 370 380 390 400
DAYTRAIRLN PYISEVWYDL GTLYETCNNQ LSDALDAYKQ AARLDVNNVH
410 420 430 440 450
IRERLEALTK QLENPGNINK SNGAPTNASP APPPVILQPT LQPNDQGNPL
460 470 480 490 500
NTRISAQSAN ATASMVQQQH PAQQTPINSS ATMYSNGASP QLQAQAQAQA
510 520 530 540 550
QAQAQAQAQA QAQAQAQAQA QAQAQAQAQA QAQAQAHAQA QAQAQAQAQA
560 570 580 590 600
QAQAQAQQQQ QQQQQQQQQQ QQQQQQQQQQ QQQQQQQLQP LPRQQLQQKG
610 620 630 640 650
VSVQMLNPQQ GQPYITQPTV IQAHQLQPFS TQAMEHPQSS QLPPQQQQLQ
660 670 680 690 700
SVQHPQQLQG QPQAQAPQPL IQHNVEQNVL PQKRYMEGAI HTLVDAAVSS
710 720 730 740 750
STHTENNTKS PRQPTHAIPT QAPATGITNA EPQVKKQKLN SPNSNINKLV
760 770 780 790 800
NTATSIEENA KSEVSNQSPA VVESNTNNTS QEEKPVKANS IPSVIGAQEP
810 820 830 840 850
PQEASPAEEA TKAASVSPST KPLNTEPESS SVQPTVSSES STTKANDQST
860 870 880 890 900
AETIELSTAT VPAEASPVED EVRQHSKEEN GTTEASAPST EEAEPAASRD
910 920 930 940 950
AEKQQDETAA TTITVIKPTL ETMETVKEEA KMREEEQTSQ EKSPQENTLP
960
RENVVRQVEE DENYDD
Length:966
Mass (Da):107,202
Last modified:October 5, 2010 - v2
Checksum:iFC2D0D0C1B181207
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti547 – 5471Q → K in AAA34545. (PubMed:2854095)Curated
Sequence conflicti547 – 5471Q → K in AAA35103. (PubMed:3316983)Curated

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M23440 Genomic DNA. Translation: AAA34545.1.
M17826 Genomic DNA. Translation: AAA35103.1.
X66247 Genomic DNA. Translation: CAA46973.1.
X78993 Genomic DNA. Translation: CAA55615.1.
Z35981 Genomic DNA. Translation: CAA85069.1.
BK006936 Genomic DNA. Translation: DAA07232.1.
PIRiS25365.
RefSeqiNP_009670.3. NM_001178460.3.

Genome annotation databases

EnsemblFungiiYBR112C; YBR112C; YBR112C.
GeneIDi852410.
KEGGisce:YBR112C.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M23440 Genomic DNA. Translation: AAA34545.1 .
M17826 Genomic DNA. Translation: AAA35103.1 .
X66247 Genomic DNA. Translation: CAA46973.1 .
X78993 Genomic DNA. Translation: CAA55615.1 .
Z35981 Genomic DNA. Translation: CAA85069.1 .
BK006936 Genomic DNA. Translation: DAA07232.1 .
PIRi S25365.
RefSeqi NP_009670.3. NM_001178460.3.

3D structure databases

ProteinModelPortali P14922.
SMRi P14922. Positions 46-395.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 32816. 103 interactions.
DIPi DIP-696N.
IntActi P14922. 10 interactions.
MINTi MINT-579675.
STRINGi 4932.YBR112C.

Proteomic databases

MaxQBi P14922.
PaxDbi P14922.
PeptideAtlasi P14922.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblFungii YBR112C ; YBR112C ; YBR112C .
GeneIDi 852410.
KEGGi sce:YBR112C.

Organism-specific databases

SGDi S000000316. CYC8.

Phylogenomic databases

eggNOGi COG0457.
GeneTreei ENSGT00410000025758.
InParanoidi P14922.
KOi K06665.
OrthoDBi EOG7NKKW1.

Enzyme and pathway databases

BioCyci YEAST:G3O-29073-MONOMER.

Miscellaneous databases

NextBioi 971258.

Gene expression databases

Genevestigatori P14922.

Family and domain databases

Gene3Di 1.25.40.10. 2 hits.
InterProi IPR013026. TPR-contain_dom.
IPR011990. TPR-like_helical_dom.
IPR001440. TPR_1.
IPR019734. TPR_repeat.
[Graphical view ]
Pfami PF00515. TPR_1. 6 hits.
[Graphical view ]
SMARTi SM00028. TPR. 10 hits.
[Graphical view ]
PROSITEi PS50005. TPR. 9 hits.
PS50293. TPR_REGION. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Cloning and characterization of the CYC8 gene mediating glucose repression in yeast."
    Trumbly R.J.
    Gene 73:97-111(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. "Molecular analysis of SSN6, a gene functionally related to the SNF1 protein kinase of Saccharomyces cerevisiae."
    Schultz J., Carlson M.
    Mol. Cell. Biol. 7:3637-3645(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  3. "Molecular analysis of yeast chromosome II between CMD1 and LYS2: the excision repair gene RAD16 located in this region belongs to a novel group of double-finger proteins."
    Mannhaupt G., Stucka R., Ehnle S., Vetter I., Feldmann H.
    Yeast 8:397-408(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  4. "Complete DNA sequence of yeast chromosome II."
    Feldmann H., Aigle M., Aljinovic G., Andre B., Baclet M.C., Barthe C., Baur A., Becam A.-M., Biteau N., Boles E., Brandt T., Brendel M., Brueckner M., Bussereau F., Christiansen C., Contreras R., Crouzet M., Cziepluch C.
    , Demolis N., Delaveau T., Doignon F., Domdey H., Duesterhus S., Dubois E., Dujon B., El Bakkoury M., Entian K.-D., Feuermann M., Fiers W., Fobo G.M., Fritz C., Gassenhuber J., Glansdorff N., Goffeau A., Grivell L.A., de Haan M., Hein C., Herbert C.J., Hollenberg C.P., Holmstroem K., Jacq C., Jacquet M., Jauniaux J.-C., Jonniaux J.-L., Kallesoee T., Kiesau P., Kirchrath L., Koetter P., Korol S., Liebl S., Logghe M., Lohan A.J.E., Louis E.J., Li Z.Y., Maat M.J., Mallet L., Mannhaupt G., Messenguy F., Miosga T., Molemans F., Mueller S., Nasr F., Obermaier B., Perea J., Pierard A., Piravandi E., Pohl F.M., Pohl T.M., Potier S., Proft M., Purnelle B., Ramezani Rad M., Rieger M., Rose M., Schaaff-Gerstenschlaeger I., Scherens B., Schwarzlose C., Skala J., Slonimski P.P., Smits P.H.M., Souciet J.-L., Steensma H.Y., Stucka R., Urrestarazu L.A., van der Aart Q.J.M., Van Dyck L., Vassarotti A., Vetter I., Vierendeels F., Vissers S., Wagner G., de Wergifosse P., Wolfe K.H., Zagulski M., Zimmermann F.K., Mewes H.-W., Kleine K.
    EMBO J. 13:5795-5809(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  5. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  6. "A repeating amino acid motif in CDC23 defines a family of proteins and a new relationship among genes required for mitosis and RNA synthesis."
    Sikorski R.S., Boguski M.S., Goebl M., Hieter P.A.
    Cell 60:307-317(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: DOMAINS TPR REPEATS.
  7. "The tetratricopeptide repeats of Ssn6 interact with the homeo domain of alpha 2."
    Smith R.L., Redd M.J., Johnson A.D.
    Genes Dev. 9:2903-2910(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH MATALPHA2.
  8. "Repression by SSN6-TUP1 is directed by MIG1, a repressor/activator protein."
    Treitel M.A., Carlson M.
    Proc. Natl. Acad. Sci. U.S.A. 92:3132-3136(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH MIG1.
  9. "The Cyc8 (Ssn6)-Tup1 corepressor complex is composed of one Cyc8 and four Tup1 subunits."
    Varanasi U.S., Klis M., Mikesell P.B., Trumbly R.J.
    Mol. Cell. Biol. 16:6707-6714(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBUNIT.
  10. "The DNA replication and damage checkpoint pathways induce transcription by inhibition of the Crt1 repressor."
    Huang M., Zhou Z., Elledge S.J.
    Cell 94:595-605(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH RFX1.
  11. "Ssn6-Tup1 interacts with class I histone deacetylases required for repression."
    Watson A.D., Edmondson D.G., Bone J.R., Mukai Y., Yu Y., Du W., Stillman D.J., Roth S.Y.
    Genes Dev. 14:2737-2744(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH TUP1; HOS2 AND RPD3, FUNCTION OF THE CYC8-TUP1 COMPLEX.
  12. "Hrs1/Med3 is a Cyc8-Tup1 corepressor target in the RNA polymerase II holoenzyme."
    Papamichos-Chronakis M., Conlan R.S., Gounalaki N., Copf T., Tzamarias D.
    J. Biol. Chem. 275:8397-8403(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH PGD1, FUNCTION OF THE CYC8-TUP1 COMPLEX.
  13. "A sequence resembling a peroxisomal targeting sequence directs the interaction between the tetratricopeptide repeats of Ssn6 and the homeodomain of alpha 2."
    Smith R.L., Johnson A.D.
    Proc. Natl. Acad. Sci. U.S.A. 97:3901-3906(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH MATALPHA2.
  14. "Regulation of the Sko1 transcriptional repressor by the Hog1 MAP kinase in response to osmotic stress."
    Proft M., Pascual-Ahuir A., de Nadal E., Arino J., Serrano R., Posas F.
    EMBO J. 20:1123-1133(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION OF THE CYC8-TUP1 COMPLEX.
  15. "SUT1p interaction with Cyc8p(Ssn6p) relieves hypoxic genes from Cyc8p-Tup1p repression in Saccharomyces cerevisiae."
    Regnacq M., Alimardani P., El Moudni B., Berges T.
    Mol. Microbiol. 40:1085-1096(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH SUT1.
  16. "Cti6, a PHD domain protein, bridges the Cyc8-Tup1 corepressor and the SAGA coactivator to overcome repression at GAL1."
    Papamichos-Chronakis M., Petrakis T., Ktistaki E., Topalidou I., Tzamarias D.
    Mol. Cell 9:1297-1305(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH CTI6.
  17. "Tup1-Ssn6 interacts with multiple class I histone deacetylases in vivo."
    Davie J.K., Edmondson D.G., Coco C.B., Dent S.Y.
    J. Biol. Chem. 278:50158-50162(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH HOS1; HOS2 AND RPD3.
  18. "Histone-dependent association of Tup1-Ssn6 with repressed genes in vivo."
    Davie J.K., Trumbly R.J., Dent S.Y.
    Mol. Cell. Biol. 22:693-703(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION OF THE CYC8-TUP1 COREPRESSOR COMPLEX.
  19. "Recruitment of Tup1-Ssn6 by yeast hypoxic genes and chromatin-independent exclusion of TATA binding protein."
    Mennella T.A., Klinkenberg L.G., Zitomer R.S.
    Eukaryot. Cell 2:1288-1303(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION OF THE CYC8-TUP1 COMPLEX.
  20. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
  21. "Large-scale phosphorylation analysis of alpha-factor-arrested Saccharomyces cerevisiae."
    Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J., Elias J.E., Gygi S.P.
    J. Proteome Res. 6:1190-1197(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-815; SER-817 AND SER-943, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Strain: ADR376.
  22. "Analysis of phosphorylation sites on proteins from Saccharomyces cerevisiae by electron transfer dissociation (ETD) mass spectrometry."
    Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L., Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F.
    Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-710, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  23. "A multidimensional chromatography technology for in-depth phosphoproteome analysis."
    Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.
    Mol. Cell. Proteomics 7:1389-1396(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-429; THR-475; SER-768; SER-866 AND SER-943, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  24. "The yeast global transcriptional co-repressor protein Cyc8 can propagate as a prion."
    Patel B.K., Gavin-Smyth J., Liebman S.W.
    Nat. Cell Biol. 11:344-349(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PRION FORMATION.
  25. "Global analysis of Cdk1 substrate phosphorylation sites provides insights into evolution."
    Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.
    Science 325:1682-1686(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-429; SER-741; SER-815; SER-817 AND SER-943, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiCYC8_YEAST
AccessioniPrimary (citable) accession number: P14922
Secondary accession number(s): D6VQB2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 1990
Last sequence update: October 5, 2010
Last modified: October 29, 2014
This is version 166 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

[OCT+] is the prion form of CYC8. [OCT+] is the result of a conformational change of the cellular CYC8 protein that becomes self-propagating and infectious. [OCT+] aggregates sequester soluble CYC8, resulting in increased levels of iso-2-cytochrome c, defects in sporulation and mating, higher levels of invertase derepression and increased flocculation, reminiscent of a partial loss of function of the CYC8-TUP1 corepressor complex. [OCT+] can be cured by GdnHCl and by inactivation of the molecular chaperone HSP104, which is required for [OCT+] propagation. It is speculated that prion properties of transcription factors may generate an optimized phenotypic heterogeneity that buffers yeast populations against diverse environmental insults (PubMed:19219034).1 Publication
Present with 3890 molecules/cell in log phase SD medium.1 Publication

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
  2. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  3. Yeast chromosome II
    Yeast (Saccharomyces cerevisiae) chromosome II: entries and gene names

External Data

Dasty 3